Methed-up FOXOs can't in-Akt-ivate.
In this issue of Molecular Cell, Yamagata et al. (2008) identify a role for the protein methyltransferase, PRMT1, in Akt-dependent regulation of the FOXO1 transcription factor and demonstrate another level of control in this critical metabolic and cell survival signaling pathway.
Michalek
Ryan D
RD
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Rathmell
Jeffrey C
JC
D021581:Active Transport, Cell Nucleus; D001120:Arginine / Q000378:metabolism; D000071161:Forkhead Box Protein O1; D051858:Forkhead Transcription Factors / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D006801:Humans; D008745:Methylation; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011484:Protein-Arginine N-Methyltransferases / Q000502:physiology; D051057:Proto-Oncogene Proteins c-akt / Q000502:physiology*; D012097:Repressor Proteins / Q000502:physiology; D015398:Signal Transduction; D054875:Ubiquitination
C085126:FOXO1 protein, human; D000071161:Forkhead Box Protein O1; D051858:Forkhead Transcription Factors; D012097:Repressor Proteins; D001120:Arginine; C099988:PRMT1 protein, human; D011484:Protein-Arginine N-Methyltransferases; D051057:Proto-Oncogene Proteins c-akt; D046988:Proteasome Endopeptidase Complex